A dansylated derivative of glucagon has been prepared and purified. Using this compound it was found that glucagon exhibits concentration dependent self-association at concentrations above 10 to the seven M. This aggregation effect was found to be dependent on the C-terminal region of the molecule. A photoaffinity derivative of glucagon has been prepared. Preliminary studies shown that it is incorporated into a protein of approximately 60,000 MW. Using a dinitrophenylated derivative of glucagon, solubilization and purification of the glucagon receptor has been attempted. A glucagon affinity column also has been prepared. The solid phase synthesis of glucagon is being attempted employing very mild synthetic and cleavage conditions. A protein kinase peptide has been synthesized in which a tryptophan residue has been introduced. This peptide shows increased fluorescence on phosphorylation, thus providing a highly sensitive assay of c-AMP-dependent protein kinase and phosphoprotein phosphatase activities.